Hydrophobic labeling of (Na+,K+)-ATPase: further evidence that the beta subunit is embedded in the membrane bilayer.


Autoria(s): Girardet M.; Geering K.; Rossier B.C.; Kraehenbuhl J.P.; Bron C.
Data(s)

1983

Resumo

O-Hexanoyl-3,5-diiodo-N-(4-azido-2-nitro-phenyl)tyramine has been used after photochemical conversion into the reactive nitrene to label (Na+,K+)-ATPase from Bufo marinus toad kidney. Immunochemical evidence indicates that the reagent labels both subunits of the enzyme in partially purified form as well as in microsomal membranes. These results support the view that the glycoprotein subunit, like the catalytic subunit, possesses hydrophobic domains by which it is integrated into the plasma membrane.

Identificador

http://serval.unil.ch/?id=serval:BIB_24EA03F7F256

isbn:0006-2960

pmid:6305414

doi:10.1021/bi00278a037

isiid:A1983QM57500037

Idioma(s)

en

Fonte

Biochemistry, vol. 22, no. 9, pp. 2296-300

Palavras-Chave #Animals; Bufo marinus; Indicators and Reagents; Kidney; Kinetics; Lipid Bilayers; Macromolecular Substances; Microsomes; Sodium-Potassium-Exchanging ATPase; Tyramine
Tipo

info:eu-repo/semantics/article

article